Difference between revisions of "Psd"
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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of phospholipids | |style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of phospholipids | ||
|- | |- | ||
| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU02290 psd] |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_synthesis.html Lipid synthesis]''' | ||
| Line 24: | Line 24: | ||
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ybfM]]'', ''[[ybfN]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ybfM]]'', ''[[ybfN]]'' | ||
|- | |- | ||
| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU02290 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU02290 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU02290 Advanced_DNA] |
|- | |- | ||
|colspan="2" | '''Genetic context''' <br/> [[Image:psd_context.gif]] | |colspan="2" | '''Genetic context''' <br/> [[Image:psd_context.gif]] | ||
Revision as of 12:02, 13 May 2013
- Description: phosphatidylserine decarboxylase
| Gene name | psd |
| Synonyms | |
| Essential | no |
| Product | phosphatidylserine decarboxylase |
| Function | biosynthesis of phospholipids |
| Gene expression levels in SubtiExpress: psd | |
| Metabolic function and regulation of this protein in SubtiPathways: Lipid synthesis | |
| MW, pI | 29 kDa, 7.27 |
| Gene length, protein length | 789 bp, 263 aa |
| Immediate neighbours | ybfM, ybfN |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
biosynthesis of lipids, cell envelope stress proteins (controlled by SigM, V, W, X, Y), membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU02290
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Phosphatidyl-L-serine = phosphatidylethanolamine + CO2 (according to Swiss-Prot)
- Protein family: Type 1 subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
- cell membrane at the septum PubMed
Database entries
- Structure:
- UniProt: P39822
- KEGG entry: [3]
- E.C. number: 4.1.1.65
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Letal I Salzberg, John D Helmann
Phenotypic and transcriptomic characterization of Bacillus subtilis mutants with grossly altered membrane composition.
J Bacteriol: 2008, 190(23);7797-807
[PubMed:18820022]
[WorldCat.org]
[DOI]
(I p)
Ayako Nishibori, Jin Kusaka, Hiroshi Hara, Masato Umeda, Kouji Matsumoto
Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes.
J Bacteriol: 2005, 187(6);2163-74
[PubMed:15743965]
[WorldCat.org]
[DOI]
(P p)
Min Cao, John D Helmann
The Bacillus subtilis extracytoplasmic-function sigmaX factor regulates modification of the cell envelope and resistance to cationic antimicrobial peptides.
J Bacteriol: 2004, 186(4);1136-46
[PubMed:14762009]
[WorldCat.org]
[DOI]
(P p)
K Matsumoto, M Okada, Y Horikoshi, H Matsuzaki, T Kishi, M Itaya, I Shibuya
Cloning, sequencing, and disruption of the Bacillus subtilis psd gene coding for phosphatidylserine decarboxylase.
J Bacteriol: 1998, 180(1);100-6
[PubMed:9422599]
[WorldCat.org]
[DOI]
(P p)
